A new strategy for caging proteins regulated by kinases

Mousumi Ghosh, Ilia Ichetovkin, Xiaoyan Song, John S. Condeelis, David S. Lawrence

Research output: Contribution to journalArticlepeer-review

43 Scopus citations


A strategy has been developed for caging proteins that are endogenously regulated by phosphorylation. A key phosphorylatable serine in cofilin, an F-actin cleaving protein, was replaced with a nonphosphorylatable cysteine. The latter conversion ensures that the protein is no longer regulated by endogenous protein kinases. The cysteine residue was subsequently covalently modified with a negatively charged caging moiety, which electrostatically mimics the natural serine phosphate present in the inactive wild-type protein. Photoremoval of the cage generates an active protein, which cannot be switched off by endogenous protein kinases. Caged cofilin, and its irradiated counterpart, display the anticipated F-actin depolymerization and severing activities.

Original languageEnglish (US)
Pages (from-to)2440-2441
Number of pages2
JournalJournal of the American Chemical Society
Issue number11
StatePublished - Mar 20 2002

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


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